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BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879

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Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,321

Redox Regulation of Cellular Signalling

Kamata, H., & Hirata, H. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(98)00037-0 · Cited by 1,162

Oxidation-reduction potentials of organic systems

(1960) · Journal of the Franklin Institute · doi:10.1016/0016-0032(60)90644-x · Cited by 889

[11] Redox potential of GSH/GSSG couple: Assay and biological significance

Jones, D. P. (2002) · Methods in Enzymology · doi:10.1016/s0076-6879(02)48630-2 · Cited by 812

Carbonyl modified proteins in cellular regulation, aging, and disease2,3 2Guest Editor: Earl Stadtman 3This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease.” The full list of papers may be found on the homepage of the journal.

Levine, R. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00765-7 · Cited by 676

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Cai, J., Nelson, K. C., Wu, M., Sternberg, P., & Jones, D. P. (2000) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(99)00009-9 · Cited by 628

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Jones, D. P., Carlson, J. L., Mody, V. C., Cai, J., Lynn, M., & Sternberg, P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00275-0 · Cited by 587

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Samiec, P. S., Drews‐Botsch, C., Flagg, E. W., Kurtz, J. C., Sternberg, P., Reed, R. L., & Jones, D. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00286-4 · Cited by 497

Glutathione measurement in human plasma

Jones, D. P., Carlson, J. L., Samiec, P. S., Sternberg, P., Mody, V. C., Reed, R. L., & Brown, L. A. S. (1998) · Clinica Chimica Acta · doi:10.1016/s0009-8981(98)00089-8 · Cited by 485

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Jackman, N. A., Melchior, S. E., Hewett, J. A., & Hewett, S. J. (2012) · ASN NEURO · doi:10.1042/an20110030 · Cited by 29

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Galli, F., Marcantonini, G., Giustarini, D., Albertini, M. C., Migni, A., Zatini, L., Gioiello, A., Rossi, R., & Bartolini, D. (2022) · Antioxidants · doi:10.3390/antiox11071366 · Cited by 29

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Salzano, G., Costa, D. F. G., & Torchilin, V. P. (2015) · Current Pharmaceutical Design · doi:10.2174/138161282131151013190410 · Cited by 27

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Ikeda-Imafuku, M., Ishima, Y., Chuang, V. T. G., Sakai, M., Osafune, H., Ando, H., Shimizu, T., Okuhira, K., Watanabe, H., Maruyama, T., et al. (2019) · Molecules · doi:10.3390/molecules24091689 · Cited by 27

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Pavão, M. L., Ferin, R., Lima, A. C. V. M. D. R., & Baptista, J. (2022) · Advances in clinical chemistry · doi:10.1016/bs.acc.2022.03.003 · Cited by 26

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Niedzwiecki, M. M., Hall, M. N., Liu, X., Slavkovich, V. N., Ilievski, V., Levy, D., Alam, S., Siddique, A. B., Parvez, F., Graziano, J. H., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.042 · Cited by 26

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Roede, J. R., Uppal, K., Liang, Y., Promislow, D., Wachtman, L. M., & Jones, D. P. (2013) · Redox Biology · doi:10.1016/j.redox.2013.06.003 · Cited by 26

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Gerna, D., Roach, T., Arc, E., Stöggl, W., Limonta, M., Vaccino, P., & Kranner, I. (2018) · Biochemical Journal · doi:10.1042/bcj20180632 · Cited by 25

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Gorąca, A., & Skibska, B. (2005) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656724 · Cited by 25

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Takemoto, H., Miyata, K., Nishiyama, N., & Kataoka, K. (2014) · Advances in genetics · doi:10.1016/b978-0-12-800148-6.00010-9 · Cited by 24

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Wada, Y., Sato, Y., Miyazaki, K., Takeda, Y., & Kuwahata, M. (2016) · Nutrition Research · doi:10.1016/j.nutres.2016.12.003 · Cited by 24

Telomere length, sibling competition and development of antioxidant defense in wild house mice

Stauffer, J., Panda, B., & Ilmonen, P. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.10.002 · Cited by 24

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Taylor, R. P., & James, T. J. (2005) · Springer eBooks · doi:10.1007/3-540-28804-x_13 · Cited by 24

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Goralski, T. M., & Ram, J. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020717 · Cited by 23

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Verbruggen, L., Ates, G., Lara, O., Munck, J. D., Villers, A., Pauw, L. D., Ottestad‐Hansen, S., Kobayashi, S., Beckers, P., Janssen, P., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01470-5 · Cited by 23

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Torrelles, J. B., Restrepo, B. I., Bai, Y., Ross, C. N., Schlesinger, L. S., & Turner, J. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.818700 · Cited by 24

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Stewart, A. N., Glaser, E. P., Mott, C. A., Bailey, W. M., Sullivan, P. G., Patel, S. P., & Gensel, J. C. (2022) · Journal of Neurotrauma · doi:10.1089/neu.2022.0010 · Cited by 22

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Rémond, D., Buffière, C., Pouyet, C., Papet, I., Dardevet, D. P., Savary‐Auzeloux, I., Williamson, G., Faure, M., & Breuillé, D. (2010) · Amino Acids · doi:10.1007/s00726-010-0672-6 · Cited by 22

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Bloom, H. L., Shukrullah, I., Veledar, E., Gutmann, R. A., London, B., & Dudley, S. C. (2010) · Cardiology Research and Practice · doi:10.4061/2010/253803 · Cited by 22

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Galván, I., Alonso‐Álvarez, C., & Negro, J. J. (2012) · Physiological and Biochemical Zoology · doi:10.1086/666606 · Cited by 22

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Sarver, D. C., Saqib, M., Chen, F., & Wong, G. W. (2024) · eLife · doi:10.7554/elife.96926.4 · Cited by 43

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Maurya, P. K., Kumar, P., Nagotu, S., Chand, S., & Chandra, P. (2016) · RSC Advances · doi:10.1039/c6ra05121a · Cited by 21

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Cumpstey, A. F., & Feelisch, M. (2017) · Wiley-VCH eBooks · doi:10.1002/9783527692156.ch27 · Cited by 22

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Lin, L., Qin, H., Huang, J., Liang, H., Quan, D., & Lu, J. (2018) · Polymer Chemistry · doi:10.1039/c8py00548f · Cited by 21

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Claeson, A., Gouveia-Figueira, S. C., Stenlund, H. C., & Johansson, A. I. (2018) · Journal of Chromatography B · doi:10.1016/j.jchromb.2018.11.007 · Cited by 21

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de Grey, A. D. (2003) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.7.1.1 · Cited by 21

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Martis, R. M., Knight, L. J., Donaldson, P. J., & Lim, J. C.-H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4594606 · Cited by 19

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Gruber, J., & Halliwell, B. B. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160091 · Cited by 20

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Jara, C., Torres, A. K., Olesen, M. A., & Tapia‐Rojas, C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88445 · Cited by 20

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Patwardhan, R. S., Singh, B., Pal, D., Checker, R., Bandekar, M., Sharma, D., & Sandur, S. K. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1745202 · Cited by 21

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Mannery, Y. O., Ziegler, T. R., Li, H., Shyntum, Y., & Jones, D. P. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00359.2009 · Cited by 19

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Bennett, S. J., & Griffiths, H. R. (2012) · Springer eBooks · doi:10.1007/978-1-4614-6166-1_2 · Cited by 19

Hepatocyte-targeting and microenvironmentally responsive glycolipid-like polymer micelles for gene therapy of hepatitis B

Miao, J., Yang, X., Shang, X., Gao, Z., Li, Q., Hong, Y. K., Wu, J., Meng, T., Yuan, H., & Hu, F. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.02.013 · Cited by 18

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Zhu, J. W., Yuan, J. F., Yang, H. M., Wang, S. T., Zhang, C. G., Sun, L., Yang, H. M., & Zhang, H. (2011) · Biochimie · doi:10.1016/j.biochi.2011.09.013 · Cited by 20

Circadian and age‐related changes in stress responsiveness of the adrenal cortex and erythrocyte antioxidant enzymes in female rhesus monkeys

Goncharova, N. D., Shmaliy, A. V., Marenin, V. Y., Smelkova, S. A., & Lapin, B. A. (2008) · Journal of Medical Primatology · doi:10.1111/j.1600-0684.2007.00278.x · Cited by 18

A study of the oxidative processes in human plasma by time-resolved fluorescence spectroscopy

Wybranowski, T., Ziomkowska, B., Cyrankiewicz, M., Bosek, M., Pyskir, J., Napiórkowska-Mastalerz, M., & Kruszewski, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-13109-0 · Cited by 17

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Borbényi-Galambos, K., Czikora, Á., Erdélyi, K., & Nagy, P. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102440 · Cited by 17

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Grunwell, J. R., Gillespie, S. E., Ward, J. M., Fitzpatrick, A. M., Brown, L. A. S., Gauthier, T. W., & Hebbar, K. (2015) · Frontiers in Pediatrics · doi:10.3389/fped.2015.00046 · Cited by 17

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Salmi, H., Leonard, J. V., Rahman, S., & Lapatto, R. (2012) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365513.2011.646299 · Cited by 17

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Cásedas, G., Bennett, A. C., González‐Burgos, E., Gómez-Serranillos, M. P., López, V., & Smith, C. (2018) · Inflammopharmacology · doi:10.1007/s10787-018-0549-y · Cited by 17

Validation of a simplified procedure for convenient and rapid quantification of reduced and oxidized glutathione in human plasma by liquid chromatography tandem mass spectrometry analysis

Enomoto, A. C., Schneider, E., McKinnon, T. A., Goldfine, H., & Levy, M. A. (2020) · Biomedical Chromatography · doi:10.1002/bmc.4854 · Cited by 17

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Zheng, Y., Merchant, M. L., Burke, T. J., Ritzenthaler, J. D., Li, M., Gawęda, A. E., Benz, F. W., Roman, J., & Watson, W. H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2468986 · Cited by 16

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Feillet‐Coudray, C., Meunier, N., Bayle, D., Brandolini-Bunlon, M., Andriollo-Sanchez, M., O’Connor, J. M., Maiani, G., Roussel, A., Mazur, A., & Coudray, C. (2006) · British Journal Of Nutrition · doi:10.1079/bjn20061762 · Cited by 17

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Brantley, M. A., Osborn, M. P., Sanders, B. J., Rezaei, K. A., Lu, P., Li, C., Milne, G. L., Cai, J., & Sternberg, P. (2012) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2011.12.010 · Cited by 16

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Douris, P. C., Elokda, A. S., Handrakis, J. P., Principal, S., Rondo, E., Bovell, J., Coughlin, W. P., Mastroianni, C. N., Wong, M. J., & Zimmerman, T. (2009) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e3181b339ac · Cited by 16

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Watson, W. H., Burke, T. J., Zelko, I. N., Torres-González, E., Ritzenthaler, J. D., & Roman, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1561305 · Cited by 17

Exercise modulation of total antioxidant capacity (TAC): towards a molecular signature of healthy aging

Ferrari, G. S. L., & Ferrari, C. K. B. (2011) · Frontiers in Life Science · doi:10.1080/21553769.2011.635008 · Cited by 19

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Ling, Y.-Y., Ren, J. M., Li, T., Zhao, Y., & Wu, C. (2016) · Chemical Communications · doi:10.1039/c6cc00369a · Cited by 16

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Babu, C. K., Ansari, K. M., Mehrotra, S., Khanna, R., Khanna, S. K., & Das, M. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.03.031 · Cited by 16

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Arif, M. U., Khan, M. K. I., Riaz, S., Nazir, A., Maan, A. A., Amin, U., Saeed, F., & Afzaal, M. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111763 · Cited by 17

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White, A. C., Sousa, A. M., Blumberg, J. B., Ryan, H., Fanburg, B. L., & Kayyali, U. S. (2006) · Bone Marrow Transplantation · doi:10.1038/sj.bmt.1705475 · Cited by 15

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Dubinina, E. E., & Васильевна, П. А. (2007) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750807040026 · Cited by 15

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Martínez, M. (2023) · Antioxidants · doi:10.3390/antiox12071373 · Cited by 14

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Priora, R., Coppo, L., Margaritis, A., Giuseppe, D. D., Frosali, S., Summa, D., Heo, J., & Simplicio, P. D. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.11.003 · Cited by 14

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del Valle, L. G., Hernández, R. G., Roche, L. D., & Fernández, O. (2015) · ACS symposium series · doi:10.1021/bk-2015-1200.ch006 · Cited by 15

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Trevisan, R., Flores-Nunes, F., Dolores, E. S., Mattos, J. J., Piazza, C. E., Sasaki, S., Taniguchi, S., Montone, R. C., Bı́cego, M. C., dos Reis, Í. M. M., et al. (2016) · Environmental Toxicology and Chemistry · doi:10.1002/etc.3543 · Cited by 14

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Kurti, S. P., Emerson, S. R., Rosenkranz, S. K., Teeman, C. S., Emerson, E. M., Cull, B. J., Smith, J. R., & Harms, C. A. (2017) · Nutrition Research · doi:10.1016/j.nutres.2017.02.003 · Cited by 14

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Bull, R. J., Kolisetty, N., Zhang, X., Muralidhara, S., Quiñones, O., Lim, K. Y., Guo, Z., Cotruvo, J. A., Fisher, J. W., Yang, X., et al. (2012) · Toxicology · doi:10.1016/j.tox.2012.06.002 · Cited by 13

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Chen, X., Lee, J., Wu, H., Tsang, A. W., & Furdui, C. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_19 · Cited by 12

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Murphy, D. D., Reddy, E. C., Moran, N. M., & O'Neill, S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5698 · Cited by 14

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Gauthier, T. W., Kable, J. A., Burwell, L., Coles, C. D., & Brown, L. A. S. (2009) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2009.01072.x · Cited by 13

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García‐de‐la‐Asunción, J., del Olmo, E. G., Galán, G., Guijarro, R., Martí, F., Badenes, R., Perez-Griera, J., Duca, A., Delgado, C., Carbonell, J., et al. (2016) · Redox Report · doi:10.1080/13510002.2015.1101890 · Cited by 13

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Martis, R. M., Donaldson, P. J., Li, B., Middleditch, M., Kallingappa, P. K., & Lim, J. C.-H. (2019) · Histochemistry and Cell Biology · doi:10.1007/s00418-019-01805-4 · Cited by 13

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Stewart, A. N., Jones, L., & Gensel, J. C. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1017153 · Cited by 13

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Triana-Martínez, F., López‐Díazguerrero, N. E., Maciel-Barón, L. Á., Morales-Rosales, S. L., Galván‐Arzate, S., Fernández, F. J., Zentella‐Dehesa, A., Pérez, V., Gómez-Quiroz, L. E., & Königsberg, M. (2013) · Biogerontology · doi:10.1007/s10522-013-9488-6 · Cited by 12

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Duong, A., Che, Y., Ceylan, D., Pinguelo, A., Andreazza, A. C., Young, L. T., & Berk, M. (2015) · Psychiatry Research · doi:10.1016/j.psychres.2015.12.015 · Cited by 12

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Watson, W. H., Greenwell, J. C., Zheng, Y., Furmanek, S. P., Torres-González, E., Ritzenthaler, J. D., & Roman, J. (2020) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2020.108431 · Cited by 12

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Jopperi-Davis, K. S. (2004) · Toxicology Letters · doi:10.1016/j.toxlet.2003.10.017 · Cited by 12

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Hunt, W. R., Hansen, J. M., & Stecenko, A. A. (2020) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2020.02.010 · Cited by 11

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Ghosh, D., & Brewer, G. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132756 · Cited by 11

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Balce, D. R., Greene, C. J., Tailor, P., & Yates, R. M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.2hi0315-083r · Cited by 11

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Cortese-Krott, M. M., & Shiva, S. (2019) · Current Opinion in Physiology · doi:10.1016/j.cophys.2019.04.016 · Cited by 11

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Jeffs, J. W., Jehanathan, N., Thibert, S. M. F., Ferdosi, S., Pham, L., Wilson, Z. T., Breburda, C. S., & Borges, C. R. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001659 · Cited by 11

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Cortese-Krott, M. M., Santolini, J., Wootton, S. A., Jackson, A. A., & Feelisch, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00004-3 · Cited by 11

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Smiljanec, K., Mbakwe, A. U., Gonzalez, M. R., Pohlig, R. T., & Lennon, S. L. (2020) · Nutrition Research · doi:10.1016/j.nutres.2020.05.011 · Cited by 9

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Zhai, L., Liang, J., Guo, X.-Q., Zhao, Y., & Wu, C. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201404909 · Cited by 9

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Tian, J. J., Brown, L. A. S., Jones, D. P., Levin, M. S., Wang, L., Rubin, D. C., & Ziegler, T. R. (2009) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607109336600 · Cited by 9

Fisetin Alleviates d -Galactose-Induced Senescence in C2C12 Myoblasts: Metabolic and Gene Regulatory Mechanisms

Zhang, Y., Wu, W., Huang, C., & Lin, D. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00939 · Cited by 9

The Evolving Concept of Oxidative Stress

Fernandes, D. D. C., Bonatto, D., & Laurindo, F. R. M. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-600-9_1 · Cited by 8

Glutathione Metabolism in Yeasts and Construction of the Advanced Producers of This Tripeptide

Kurylenko, O. O., Dmytruk, K. V., & Sibirny, A. А. (2019) · Springer eBooks · doi:10.1007/978-3-030-21110-3_6 · Cited by 7

Tracking the Stability of Clinically Relevant Blood Plasma Proteins with Delta-S-Cys-Albumin—A Dilute-and-Shoot LC/MS-Based Marker of Specimen Exposure to Thawed Conditions

Kapuruge, E. P., Jehanathan, N., Rogers, S. P., Williams, S. A., Chung, Y., & Borges, C. R. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100420 · Cited by 8

The correlations between oxidative stress markers and indoor volatile organic compounds among the general population in Ansan and Incheon cities, Korea

Hong, E., Lee, E., Kim, Y., Oh, E., Kim, Y. W., Moon, K. W., Choi, J. W., Lee, J., & Roh, J. Y. (2009) · Toxicology and Environmental Health Sciences · doi:10.1007/bf03216462 · Cited by 8

Age-related alterations of plasma glutathione and oxidation of redox potentials in chimpanzee (Pan troglodytes) and rhesus monkey (Macaca mulatta)

Paredes, J., Jones, D. P., Wilson, M. E., & Herndon, J. G. (2014) · AGE · doi:10.1007/s11357-014-9615-6 · Cited by 8

Protective effect of sulfurous water in peripheral blood mononuclear cells of Alzheimer's disease patients

Guzmán, R., Campos, C., Yuguero, R., Masegù, C., Gil, P., & Moragón, Á. C. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.04.006 · Cited by 8

Dwa oblicza wolnych rodników tlenowych The two faces of reactive oxygen species

Janusz, M. (2008) · Cited by 8

Donor factors and risk of primary graft dysfunction and mortality post lung transplantation: A proposed conceptual framework

Subramani, M. V., Nunley, D. R., & Roman, J. (2021) · Clinical Transplantation · doi:10.1111/ctr.14480 · Cited by 10

Sulfur amino acid-free diet results in increased glutamate in human midbrain: A pilot magnetic resonance spectroscopic study

Park, Y. H., Zhao, T., Gletsu-Miller, N. A., Kim, S. B., Accardi, C. J., Ziegler, T. R., Hu, X. P., & Jones, D. P. (2011) · Nutrition · doi:10.1016/j.nut.2011.05.007 · Cited by 8

Plasma Cystine Levels and Cardiovascular and All‐Cause Mortality in Hemodialysis Patients

Suzuki, S., Shino, M., Fujikawa, T., Ito, Y., Ueda, E., Hashimoto, T., Kuji, T., Kobayashi, N., Ohnishi, T., Hirawa, N., et al. (2018) · Therapeutic Apheresis and Dialysis · doi:10.1111/1744-9987.12669 · Cited by 7

The Unveiling of Therapeutic Targets for Alzheimer’s Disease: An Integrative Review

Madar, P. R., Nagalapur, P. P., Chaudhari, S. Y., Sharma, D., Koparde, A. A., Buchade, R. S., Kshirsagar, S. S., Uttekar, P. S., Jadhav, S. B., & Chaudhari, P. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266282492240220101049 · Cited by 7

L-Cysteine Upregulates Testosterone Biosynthesis and Blood–Testis Barrier Genes in Cultured Human Leydig Cells and THP-1 Monocytes and Increases Testosterone Secretion in Human Leydig Cells

Margret, J. J., & Jain, S. K. (2024) · Biomolecules · doi:10.3390/biom14091171 · Cited by 7

Free Cysteine Modulates the Conformation of Human C/EBP Homologous Protein

Singh, V. K., Rahman, M. N., Munro, K. A., Uversky, V. N., Smith, S. P., & Jia, Z. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034680 · Cited by 7

The role of physiological elements in future therapies of rheumatoid arthritis. III. The role of the electromagnetic field in regulation of redox potential and life cycle of inflammatory cells*

Gajewski, M., Rzodkiewicz, P., Maśliński, S., & Wojtecka-Lukasik, E. (2015) · Reumatologia/Rheumatology · doi:10.5114/reum.2015.54000 · Cited by 7

Transsulfuration metabolites and the association with incident atrial fibrillation – An observational cohort study among Norwegian patients with stable angina pectoris

Svenningsson, M. M., Svingen, G. F. T., Lysne, V., Ueland, P. M., Tell, G. S., Pedersen, E. R., Dhar, I., Nilsen, D. W. T., & Nygard, O. K. (2020) · International Journal of Cardiology · doi:10.1016/j.ijcard.2020.05.010 · Cited by 7

Biochemically Tracked Variability of Blood Plasma Thawed-State Exposure Times in a Multisite Collection Study

Hu, Y., Mulot, C., Bourreau, C., Martin, D., Laurent‐Puig, P., Radoï, L., Guénel, P., & Borges, C. R. (2020) · Biopreservation and Biobanking · doi:10.1089/bio.2019.0137 · Cited by 7

Influences of Occupational Burnout and Personality on Lipid Peroxidation Among Nurses in Shahroud City, Iran

Biganeh, J., Abolghasemi, J., Alimohammadi, I., EBRAHIMI, H., DAVOUD, B., Hosseinabadi, M. B., & Ashtarinezhad, A. (2021) · Journal of UOEH · doi:10.7888/juoeh.43.397 · Cited by 7

Oxidative Stress and Protein Oxidation

Grune, T., Catalgol, B., & Jung, T. (2012) · Wiley eBooks · doi:10.1002/9781118493038.ch1 · Cited by 7

Causality of Aging Hallmarks

Huang, B., & Hu, X. (2025) · Aging and Disease · doi:10.14336/ad.2025.0541 · Cited by 8

Redirecting Intermediary Metabolism to Counteract Cyanide Poisoning

Bebarta, V., & Nath, A. K. (2025) · The FASEB Journal · doi:10.1096/fj.202400230rr · Cited by 6

Extracellular Redox State: Refining the Definition of Oxidative Stress in Aging

Jones, D. P. (2006) · Rejuvenation Research · doi:10.1089/rej.2006.9.169 · Cited by 243

Age-related changes of the redox state of glutathione in plasma.

Wang, Q., Wang, S., Ding, Y., Peng, K.-J., Lin, X., Qiao, X.-R., Liu, Y., & Wu, C.-H. (2005) · PubMed · Cited by 6

Aging-related changes in the thiol/disulfide redox state: implications for the use of thiol antioxidants

Dröge, W. (2002) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00175-4 · Cited by 217

l -Cysteine Efflux in Erythrocytes As A Function of Human Age: Correlation with Reduced Glutathione and Total Anti-Oxidant Potential

Kumar, P., & Maurya, P. K. (2013) · Rejuvenation Research · doi:10.1089/rej.2012.1394 · Cited by 47

l-2-oxothiazolidine-4-carboxylate influence on age- and heat exposure-dependent redox changes in rat’s blood plasma

Hadzi‐Petrushev, N., Јankulovski, N., Hristov, K., & Mladenov, M. I. (2011) · The Journal of Physiological Sciences · doi:10.1007/s12576-011-0165-8 · Cited by 15